Role of β-turn residues in β-hairpin formation and stability in designed peptides
✍ Scribed by Marina Ramı́rez-Alvarado; Francisco J Blanco; Hartmut Niemann; Luis Serrano
- Book ID
- 115628193
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 383 KB
- Volume
- 273
- Category
- Article
- ISSN
- 0022-2836
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📜 SIMILAR VOLUMES
## Abstract The β turn segment in designed peptide hairpins has been expanded by the insertion of β‐, γ‐ and δ‐amino acids at the __i__+2 position. The model octapeptides Boc‐Leu‐Phe‐Val‐^D^Pro‐Ac~6~c‐Leu‐Phe‐Val‐OMe (1), Boc‐Leu‐Phe‐Val‐^D^Pro‐β^3^‐Ac~6~c‐Leu‐Phe‐Val‐OMe (2), and Boc‐Leu‐Phe‐Val‐^
## Abstract The structural properties of a 10‐residue and a 15‐residue peptide in aqueous solution were investigated by molecular dynamics simulation. The two designed peptides, SYINSDGTWT and SESYINSDGTWTVTE, had been studied previously by NMR at 278 K and the resulting model structures were class